EphB6 _ EPHB6 Antibody (Antigen Affinity Purified)
- Known as:
- EphB6 _ EPHB6 Antibody (Antigen Affinity Purified)
- Catalog number:
- 10197-RP02
- Product Quantity:
- 100
- Category:
- -
- Supplier:
- Smart Serology
- Gene target:
- EphB6 _ EPHB6 Antibody (Antigen Affinity Purified)
Related genes to: EphB6 _ EPHB6 Antibody (Antigen Affinity Purified)
- Gene:
- EPHB6 NIH gene
- Name:
- EPH receptor B6
- Previous symbol:
- -
- Synonyms:
- HEP
- Chromosome:
- 7q34
- Locus Type:
- gene with protein product
- Date approved:
- 1997-10-10
- Date modifiied:
- 2016-10-05
Related products to: EphB6 _ EPHB6 Antibody (Antigen Affinity Purified)
Related articles to: EphB6 _ EPHB6 Antibody (Antigen Affinity Purified)
- Pseudokinase domains (PsKDs) mediate key signaling processes involved in human disease. Despite transformative success in targeting catalytically active protein kinases, drug development for pseudokinases has lagged behind. Although they lack catalytic activity, pseudokinases are conformationally dynamic and are thought to function by switching between conformations that bind different signaling partners. This conformational switching model suggests the possibility of modulating pseudokinase signaling using small molecules that alter or bias conformational transitions. Focusing on the three PsKDs in receptor tyrosine kinases (RTKs) that retain nucleotide binding (ErbB3, EphB6, and EphA10), we used hydrogen-deuterium exchange mass spectrometry (HDX-MS) to ask whether different small molecules can promote distinct changes in conformation or dynamics. We detected distinct conformational effects in different locations within the PsKDs when different small molecules bind their respective ATP-binding sites. Our results suggest that similar small molecules will be useful probes for understanding pseudokinase function and ultimately for developing possible therapeutics. - Source: PubMed
Publication date: 2026/09/18
Sheetz Joshua BTsutsui YukoAshtekar Kumar DMathea SebastianKnapp StefanLemmon Mark A - - Source: PubMed
Publication date: 2026/09/03
- Pachymic acid (PA) is a natural active component of Poria cocos(Schw.)Wol. Although PA exhibits antitumor activity in multiple cancers, its effects and mechanisms against glioma remain elusive. This study aimed to investigate the anti-glioma effects of PA and identify its potential candidate core targets and pathways. Functional experiments demonstrated that PA significantly inhibited the proliferation, migration, and invasion of glioma cells and induced apoptosis in a dose-dependent manner. Using network pharmacology, machine learning, and bioinformatics analysis, we screened six candidate targets: PDE4D, CAPN2, MAPK9, EPHB6, CCKBR, and FAAH. TCGA analysis confirmed that CAPN2 and PDE4D were upregulated in glioma, while the others were downregulated. Molecular docking, an in silico predictive approach, suggested that PA may potentially form favorable binding conformations with these core targets based on calculated binding energies. Further verification revealed that PA treatment was associated with reduced AKT and mTOR phosphorylation, suggesting that the PI3K-AKT-mTOR pathway may be involved in mediating its anti-glioma activity. In conclusion, PA exerts dose-dependent anti-glioma cellular effects through multi-gene regulation, and the suppressed activation of the PI3K-AKT pathway may correlate with its anti-tumor function. These results provide a theoretical basis for developing PA as a potential therapeutic agent for glioma. - Source: PubMed
Publication date: 2026/07/17
Zhang MinLiu YingyanLi ZhijianZhang XiangrongCui HairuiTian JianingYang Jiankai - Receptor tyrosine pseudokinases comprise approximately 10% of the receptor tyrosine kinase family and lack phosphotransferase activity due to substitutions of essential catalytic residues within their kinase folds. This review critically examines the eight human receptor tyrosine pseudokinases: EphA10, EphB6, HER3, PTK7, ROR1, ROR2, RYK, and STYK1. By reconciling recent structural and functional data, we highlight the diverse non-catalytic mechanisms these pseudokinases employ in cellular communication. This comprehensive analysis provides insights into non-canonical signalling pathways and highlights potential for therapeutic opportunities in diseases associated with pseudokinase dysfunction. - Source: PubMed
Park Emily CThompson Andrew PMurphy James MLiang Lung-YuLucet Isabelle S - Seven in absentia homologue 2 (SIAH2) has been shown to contribute to the progression of various human tumors, including hepatocellular carcinoma (HCC). However, the precise mechanisms by which SIAH2 promotes HCC cell migration remain to be fully elucidated. In this study, we demonstrate that SIAH2 accelerates the invasion and migration of HCC cells by promoting K48-linked polyubiquitination and degradation of EPH receptor B6 (EPHB6). Notably, the invasion and migration of HCC cells regulated by the SIAH2-EPHB6 axis in association with enhanced filopodia formation, a critical early step in cell motility. Furthermore, our findings indicate that the SIAH2-EPHB6 axis promotes filopodia formation in HCC cells by modulating Ras homolog family member F (RHOF). Finally, we investigated the expression correlations among SIAH2, EPHB6, and RHOF using clinical tissue specimens. In summary, SIAH2 accelerates K48-linked polyubiquitination and degradation of EPHB6 to regulate filopodia formation in HCC cells. - Source: PubMed
Publication date: 2026/04/26
Hu QingheWu KaiLiu ZhiyiXu JiaweiYang WeichaoXia NanHou TianqiZhu YunCao KuanShi HengliangHe YiZhang Bin